Date

June 2011

Document Type

Thesis

Degree Name

M.S.

Institution

Oregon Health & Science University

Abstract

Since manganese is the second most abundant redox active transition metal after iron in the crust of the Earth, it has a large significance in terms of biogeochemical cycling. The bacteria that oxidize manganese are ubiquitous in many ecosystems, but the cellular function of oxidation is currently unknown. The enzymes within the bacteria that perform this chemistry have also been elusive in their identification. A new class of Mn(II) oxidizing peroxidase (MopA) has been discovered in Aurantimonas manganoxydans SI85-9A1, the first such peroxidases found in bacteria. Chemical assays of the loosely bound outer membrane proteins of A. manganoxydans SI85-9A1 suggest a eme peroxidase is involved with Mn(II) oxidation, although its exact role is not known. Functional assays and structural predictions provide some interesting insights into its possible use in Mn(II) oxidation as related to similar proteins. Through tri-parental mating with an E. coli donor, it was possible to incorporate the p

Identifier

doi:10.6083/M4X06510

Division

Institute of Environmental Health

School

School of Medicine

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